A three‐dimensional structure model of the complex of glutamyl‐tRNA synthetase and its cognate tRNA

FEBS Letters

Tateno, Masaru²  Nureki, Osamu²  Yokoyama, Shigeyuki²  G, Mitiko¹  Kaneda, Kazuaki¹  Sekine, Shun-ichi² 

[1] Department of Biology, Faculty of Science, Nagoya University, Nagoya, 464-01, Japan;Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Tokyo 113, Japan

关键词: Aminoacyl-tRNA synthetase;    Computer modeling;    Molecular mechanics;    Molecular superposition;    GluRS;    glutamyl-tRNA synthetase;    aaRS;    aminoacyltRNA synthetase;    GlnRS;    glutaminyl-tRNA synthetase;   

DOI  :  10.1016/0014-5793(95)01295-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A docking model of glutamyl-tRNA synthetase (GluRS) and tRNA^Glu was constructed, on the basis of the distinguished similarity between the X-ray crystallographic three-dimensional structures of the N-terminal halves of the Thermus thermophilus GluRS in the free state and the Escherichia coli glutaminyl-tRNA synthetase in a complex with tRNA^Gln. The modeled structure is energetically favorable and is also well consistent with the results of site-directed mutagenesis studies. The model indicates that the GluRS-specific insertions 2 and 3 fit and bind to the acceptor stem and the D arm, respectively, of the cognate tRNA without affecting other contacts. In particular, insertion 3 strongly interacts with the two D-stem base pairs that are essential for the tRNA·GluRS recognition.

【 授权许可】

Unknown